MSS1_YEAST
ID MSS1_YEAST Reviewed; 526 AA.
AC P32559; D6VZJ7; Q0PHA7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=tRNA modification GTPase MSS1, mitochondrial;
DE Flags: Precursor;
GN Name=MSS1; Synonyms=PET53; OrderedLocusNames=YMR023C; ORFNames=YM9711.13C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8392589; DOI=10.1006/jmbi.1993.1371;
RA Decoster E., Vassal A., Faye G.;
RT "MSS1, a nuclear-encoded mitochondrial GTPase involved in the expression of
RT COX1 subunit of cytochrome c oxidase.";
RL J. Mol. Biol. 232:79-88(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Li X., Wang X., Guan M.-X.;
RT "MSS1, a mitochondrial GTP-binding protein involved in mitochondrial tRNA
RT modification.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP INTERACTION WITH MTO1.
RX PubMed=9774408; DOI=10.1074/jbc.273.43.27945;
RA Colby G., Wu M., Tzagoloff A.;
RT "MTO1 codes for a mitochondrial protein required for respiration in
RT paromomycin-resistant mutants of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:27945-27952(1998).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=15509579; DOI=10.1074/jbc.m409306200;
RA Umeda N., Suzuki T., Yukawa M., Ohya Y., Shindo H., Watanabe K., Suzuki T.;
RT "Mitochondria-specific RNA-modifying enzymes responsible for the
RT biosynthesis of the wobble base in mitochondrial tRNAs. Implications for
RT the molecular pathogenesis of human mitochondrial diseases.";
RL J. Biol. Chem. 280:1613-1624(2005).
CC -!- FUNCTION: GTPase involved in the 5-carboxymethylaminomethyl
CC modification (mnm(5)s(2)U34) of the wobble uridine base in
CC mitochondrial tRNAs. Involved in the expression of cytochrome c oxidase
CC subunit 1 (COX1). Works in association with the small subunit of
CC mitoribosomes. {ECO:0000269|PubMed:15509579}.
CC -!- SUBUNIT: Forms a heterodimer with MTO1.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. TrmE GTPase family. {ECO:0000305}.
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DR EMBL; X69481; CAA49238.1; -; Genomic_DNA.
DR EMBL; DQ834923; ABG77646.1; -; Genomic_DNA.
DR EMBL; Z49211; CAA89126.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09921.1; -; Genomic_DNA.
DR PIR; S54025; S54025.
DR RefSeq; NP_013736.1; NM_001182519.1.
DR AlphaFoldDB; P32559; -.
DR SMR; P32559; -.
DR BioGRID; 35194; 346.
DR DIP; DIP-5882N; -.
DR IntAct; P32559; 2.
DR MINT; P32559; -.
DR STRING; 4932.YMR023C; -.
DR MaxQB; P32559; -.
DR PaxDb; P32559; -.
DR PRIDE; P32559; -.
DR EnsemblFungi; YMR023C_mRNA; YMR023C; YMR023C.
DR GeneID; 855037; -.
DR KEGG; sce:YMR023C; -.
DR SGD; S000004625; MSS1.
DR VEuPathDB; FungiDB:YMR023C; -.
DR eggNOG; KOG1191; Eukaryota.
DR GeneTree; ENSGT00390000016851; -.
DR HOGENOM; CLU_019624_3_1_1; -.
DR InParanoid; P32559; -.
DR OMA; CEIQCHG; -.
DR BioCyc; MetaCyc:G3O-32728-MON; -.
DR BioCyc; YEAST:G3O-32728-MON; -.
DR PRO; PR:P32559; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32559; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; ISS:SGD.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0070899; P:mitochondrial tRNA wobble uridine modification; IMP:SGD.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR CDD; cd04164; trmE; 1.
DR Gene3D; 1.20.120.430; -; 1.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00379; GTPase_MnmE; 1.
DR InterPro; IPR031168; G_TrmE.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR018948; GTP-bd_TrmE_N.
DR InterPro; IPR004520; GTPase_MnmE.
DR InterPro; IPR027368; MnmE_dom2.
DR InterPro; IPR025867; MnmE_helical.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF12631; MnmE_helical; 1.
DR Pfam; PF10396; TrmE_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51709; G_TRME; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..526
FT /note="tRNA modification GTPase MSS1, mitochondrial"
FT /id="PRO_0000035781"
FT DOMAIN 274..444
FT /note="TrmE-type G"
FT BINDING 281..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 328..332
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 394..397
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT CONFLICT 53
FT /note="A -> R (in Ref. 1; CAA49238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 58352 MW; 8740A374CA1E637D CRC64;
MNSASFLQSR LISRSFLVRR SLKRYSGLAK PYTFQQPTIY ALSTPANQTS AIAIIRISGT
HAKYIYNRLV DSSTVPPIRK AILRNIYSPS SCSVKPHDQK ESKILLDTSL LLYFQAPYSF
TGEDVLELHV HGGKAVVNSI LKAIGSLHDR SSGKDIRFAL PGDFSRRAFQ NGKFDLTQLE
GIKDLIDSET ESQRRSALSS FNGDNKILFE NWRETIIENM AQLTAIIDFA DDNSQEIQNT
DEIFHNVEKN IICLRDQIVT FMQKVEKSTI LQNGIKLVLL GAPNVGKSSL VNSLTNDDIS
IVSDIPGTTR DSIDAMINVN GYKVIICDTA GIREKSSDKI EMLGIDRAKK KSVQSDLCLF
IVDPTDLSKL LPEDILAHLS SKTFGNKRII IVVNKSDLVS DDEMTKVLNK LQTRLGSKYP
ILSVSCKTKE GIESLISTLT SNFESLSQSS ADASPVIVSK RVSEILKNDV LYGLEEFFKS
KDFHNDIVLA TENLRYASDG IAKITGQAIG IEEILDSVFS KFCIGK
